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Information on EC 1.1.1.250 - D-arabinitol 2-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.250
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.250 D-arabinitol 2-dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.250
-
candidiasis
- candida
- xylitol
- dehydrogenases
- polyols
- ribitol
- albicans
- l-arabinitol
-
roche
-
polyhydric
-
klebsiella
- d-mannitol
-
fluorometric
- stipitis
-
pichia
- tropicalis
- d-fructose
- d-xylulose
-
cobas
-
diagnose
-
nad-dependent
- pentitol
- pneumoniae
- galactitol
- synthesis
- analysis
showSynonyms
d-arabinitol dehydrogenase, arabitol 2-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ArDH
-
-
-
-
D-arabinitol 2-dehydrogenase (ribulose-forming)
-
-
-
-
D-arabinitol dehydrogenase
-
-
-
-
D-arabitol 2-dehydrogenase
dehydrogenase, D-arabinitol (Candida albicans clone pEMBLYe23 gene arDH reduced)
-
-
-
-
NAD-dependent arabitol dehydrogenase (Candida albicans clone pEMBLYe23)
-
-
-
-
TM_0297
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinitol + NAD+ = D-ribulose + NADH + H+
in the reverse reaction the enzyme catalyzes transfer of 4(S) hydrogen of NADH
-
D-arabinitol + NAD+ = D-ribulose + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
D-arabinose degradation V
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SYSTEMATIC NAME
IUBMB Comments
D-arabinitol:NAD+ 2-oxidoreductase (D-ribulose-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
336883-93-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-xylulose + NADH
?
-
Substrates: 1% of the activity with D-ribulose
Products: -
Products: -
?
Galactitol + NAD+
?
-
Substrates: 1.6% of the activity with D-arabinitol
Products: -
Products: -
?
L-Xylulose + NADH
?
-
Substrates: 3% of the activity with D-ribulose
Products: -
Products: -
?
Xylitol + NAD+
?
-
Substrates: 5% of the activity with D-arabinitol
Products: -
Products: -
?
D-arabitol + NAD+
D-ribulose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-arabitol + NAD+
D-ribulose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-ribulose + NADH
D-arabinitol + NAD+
-
Substrates: catalyzes the final step in the synthesis of D-arabinitol
Products: -
Products: -
?
D-ribulose + NADH
D-arabinitol + NAD+
-
Substrates: catalyzes the final step in the synthesis of D-arabinitol
Products: -
Products: -
?
D-ribulose + NADH + H+
D-arabitol + NAD+
Substrates: -
Products: -
Products: -
?
D-ribulose + NADH + H+
D-arabitol + NAD+
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
D-xylulose + NADH + H+
D-xylitol + NAD+
Substrates: -
Products: -
Products: -
?
D-xylulose + NADH + H+
D-xylitol + NAD+
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribulose + NADH
D-arabinitol + NAD+
-
Substrates: catalyzes the final step in the synthesis of D-arabinitol
Products: -
Products: -
?
D-ribulose + NADH
D-arabinitol + NAD+
-
Substrates: catalyzes the final step in the synthesis of D-arabinitol
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity
Mg2+
additional information
no effect on the activity is observed with CaCl2 or NaCl addition, up to 150 mM
Mg2+
55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.069
NAD+
85°C, pH 8.5, Strep-tagged enzyme, cosubstrate D-arabitol
0.027
NADH
85°C, pH 7.5, Strep-tagged enzyme, cosubstrate D-ribulose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
oxidation of D-arabitol is not observed below pH 4.5 or above pH 9.5
5.5 - 8.5
pH 5.5: about 40% of maximal activity, pH 8.5: about 10% of maximal activity, reduction of D-ribulose
8 - 11
-
pH 8.0: about 40% of maximal activity, pH 8.5: about 60% of maximal activity, pH 10-11: maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (936 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homododecamer
homohexamer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
85
the tag-less protein is thermostable, retaining 90% of its activity after 90 min. The Strep-tagged enzyme loese 60% of its activity after 10 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
K+, 60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity
Mg2+, 55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from Escherichia coli with and without a Strep-tag. The tag-less form of D-arabitol dehydrogenase has similar kinetic parameters compared to the tagged enzyme, demonstrating that the Strep-tag is not deleterious to protein function but decreases protein stability
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the specificity of the enzyme makes it useful for the development of a simple and specific method for the measurement of D-arabinitol, a metabolite of the pathogenic Candida spp. which has been described as a marker for disseminated candidiasis
synthesis
synthesis
the enzyme catalyzed oxidation of D-arabitol to D-ribulose which is a rare ketopentose sugar that has numerous industrially applications. D-Arabitol 2-dehydrogenase from Thermotoga maritima has the potential to be a useful biocatalyst for the production of D-ribulose starting from the inexpensive D-arabitol due to its regiospecificity and thermostability
synthesis
-
the enzyme catalyzed oxidation of D-arabitol to D-ribulose which is a rare ketopentose sugar that has numerous industrially applications. D-Arabitol 2-dehydrogenase from Thermotoga maritima has the potential to be a useful biocatalyst for the production of D-ribulose starting from the inexpensive D-arabitol due to its regiospecificity and thermostability
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wong, B.; Murray, J.S.; Castellanos, M.; Croen, K.D.
D-Arabitol metabolism in Candida albicans: studies of the biosynthetic pathway and the gene that encodes NAD-dependent D-arabitol dehydrogenase
J. Bacteriol.
175
6314-6320
1993
Candida albicans
brenda
Quong, M.W.; Miyada, C.G.; Switchenko, A.C.; Goodman, T.C.
Identification, purification, and characterization of a D-arabinitol-specific dehydrogenase from Candida tropicalis
Biochem. Biophys. Res. Commun.
196
1323-1329
1993
Candida tropicalis
brenda
Kallnik, V.; Schultz, C.; Schweiger, P.; Deppenmeier, U.
Properties of recombinant Strep-tagged and untagged hyperthermophilic D-arabitol dehydrogenase from Thermotoga maritima
Appl. Microbiol. Biotechnol.
90
1285-1293
2011
Thermotoga maritima (Q9WYD3), Thermotoga maritima DSM 3109 (Q9WYD3)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.250)
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